PMID: 8611654Apr 12, 1996Paper

Five isoenzymes of protein kinase C are expressed in normal and STZ-diabetic rat hepatocytes: effect of phorbol 12-myristate 13-acetate

Biochimica Et Biophysica Acta
F CroquetJ Féger

Abstract

Using isoenzyme-specific antisera, five Protein Kinase Cs (PKCs) were detected in cytosol and membrane hepatocytes from normal rats: PKC alpha (80 kDa), PKC beta II (40, 50, 55, 85 kDa), PKC delta (74, 76 kDa), PKC epsilon (95 kDa), PKC zeta (65, 70 kDa). STZ-diabetes induced a lower expression of the five PKCs, a higher localization in the cytosol, a preferential expression of PKC delta as the 76 kDa phosphorylated species and a decreased kinase activity towards Histone III-S. A 1 microM phorbol 12-myristate 13-acetate (PMA) incubation induced similar translocation to the membrane of PKCs alpha, native 85 kDa beta II and epsilon. The 74 kDa PKC delta was switched to the 76 kDa species, the normal form in STZ-diabetic cells. The truncated PKC beta II and PKC epsilon were unchanged.

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Citations

Dec 18, 2003·Toxicology and Applied Pharmacology·Liliane-Eustache OkoumassounFrancine Denizeau
May 9, 2008·American Journal of Physiology. Cell Physiology·Behnam SaberiDerick Han
Oct 31, 2008·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Fernando A CrocenziMary Vore
Jul 23, 2013·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Behnam SaberiNeil Kaplowitz
Dec 19, 2008·Biological Chemistry·Claudia StrossRalf Kubitz
Dec 18, 2003·The Journal of Biological Chemistry·Ralf KubitzDieter Häussinger

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